1980
DOI: 10.1002/jsfa.2740310403
|View full text |Cite
|
Sign up to set email alerts
|

The determination of trypsin inhibitor levels in foodstuffs

Abstract: The trypsin inhibitor activity of processed foods can be determined by measuring the loss of activity of added trypsin under standard conditions. Observed values are not usually independent of the degree of inhibition, and averaging over a range of inhibition levels or extrapolation to zero inhibition may not produce a more reliable value. A somewhat modified method is described which has been tested in two laboratories and used for large numbers of different samples on a routine basis; its application and lim… Show more

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
3
1
1

Citation Types

4
177
4
4

Year Published

1997
1997
2019
2019

Publication Types

Select...
9

Relationship

0
9

Authors

Journals

citations
Cited by 319 publications
(189 citation statements)
references
References 8 publications
4
177
4
4
Order By: Relevance
“…The data are expressed as amount of protease inhibited per amount of sample material. As Kakade et al [16] and Smith et al [17] pointed out, such values prevent the confusion that arises from using arbitrary values and allow the amount of inhibitory activity to be more easily appreciated by non-analists. The procedure that is described above differs in several aspects from previous methods.…”
Section: Discussionmentioning
confidence: 99%
See 1 more Smart Citation
“…The data are expressed as amount of protease inhibited per amount of sample material. As Kakade et al [16] and Smith et al [17] pointed out, such values prevent the confusion that arises from using arbitrary values and allow the amount of inhibitory activity to be more easily appreciated by non-analists. The procedure that is described above differs in several aspects from previous methods.…”
Section: Discussionmentioning
confidence: 99%
“…PPI is highly soluble under these conditions. While alkaline conditions like those used by Kakade et al [18], Stauffer [19] and Smith et al [17] also favour PPI solubility, these were avoided to prevent oil and fat hydrolysis as free fatty acids may also inhibit trypsin.…”
Section: Discussionmentioning
confidence: 99%
“…The phytic acid content was calculated from a calibration curve using phytate phosphorus salt in the range of 10-50 lg. Trypsin inhibitor activity (TIA) was determined colorimetrically using a spectrophotometer at 410 nm (Smith et al 1980).…”
Section: Chemical Analysismentioning
confidence: 99%
“…Tannin determination was by method of Makkar and Goodchild (1996); phytate by method of Wheeler and Ferrel (1971), while trypsin inhibition was by method of Kakade et al (1969), as modified by Smith et al (1980). …”
Section: Antinutritional Analysesmentioning
confidence: 99%